The development of ultrafast kinetic methods is one of the factors that allowed the research on protein folding to flourish over the last 20 years. The introduction of new optical triggering techniques enabled to experimentally investigate the protein dynamics at the nanosecond to millisecond timescale, allowing researchers to test theoretical predictions and providing experimental benchmarks for computer simulations. In this work, the details of how to perform kinetic experiments by the laser-induced temperature-jump technique, using the two most commonly used probing techniques (namely infrared absorption and fluorescence spectroscopy) are given, with a strong emphasis on the practical details.
Keywords: Fluorescence; Folding kinetics; Förster resonance energy transfer; Infrared absorption; Protein folding; Pump and probe; Temperature jump.
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